FGSC #8387

Mutant Type

Genus: N

reporting_genes: his-3; aga

species: Neurospora crassa

allele: Y155M261;UM906

stock: 2747-22a

glasgow:

mutagen:

Depositor: RHD

Link Group: IR; VIIR

MT: a

Species No: 10

gene_back:

oppmt:

trans:

ref1: Hoyt et al 2000 Mol Cell Biol, 20:2760-2773, https://doi.org/10.1128/mcb.20.8.2760-2773.2000

ref2:

site:

country:

ksudc_link: https://digital.lib.k-state.edu/item/neurospora-crassa/fgsc-8387

ksudc_link_html: https://digital.lib.k-state.edu/item/neurospora-crassa/fgsc-8387 ↗

Genes

Locus	Cultural Requirements	Link Group	Type
his-3	IR. Right of met-10 (R.L. Metzenberg, personal communication). Left of cog (1 to 3%) (172,174), ure-4 (1%) (78), and ad-3A (1%) (271). (434)Requires histidine (434). Complex gene coding for histidinol dehydrogenase, phosphoribosyladenosine 5'-triphosphate-pyrophosphohydrolase, and phosphoribosyl-adenosine 5'-monophosphate-cyclohydrolase (16, 673) (Fig. 14). All three activities appear to be catalyzed by a single protein (673). Strains carrying different individual alleles may lack only the early reaction(s) or only histidinol dehydrogenase, or both. Those that lack only histidinol dehydrogenase accumulate histidinol (16, 162, 1123). Mutants produce cross-reacting material (220). Used to study intralocus complementation and recombination (15, 16, 27, 162, 164, 171, 172, 1121, 1122, 1124). Intralocus recombination is regulated by cog and by rec-2 (27, 171); it is not affected by rec-1 (172). Translocation T(IR;VII)TM429, with one breakpoint in his-3, has been used to show that cog is cis-acting (171). Initial alleles: C140 and T1710 (= C1710).	IR	B
aga	VIIR. Between wc-1 (2%) and arg-10 (24 to 27%) (240, 697). Presumed structural gene for arginase (240, 697) (see Fig. 10). Unable to form ornithine from arginine; arginine is thus unable to satisfy the proline requirement of pro-3 in a pro-3 aga double mutant. Prototrophic single mutants develop polyamine requirement in the presence of arginine. This is due to feedback inhibition of ornithine biosynthesis by arginine, combined with a catabolic block in ornithine formation from arginine (240). Siderophore production is severely reduced in the absence of ornithine in the triple mutant aga arg-5 ota, which has been used to study iron transport (1146, 1147) and to obtain mutants defective in siderophore uptake (G.W. Charlang and N.P. Williams, personal communication); see sit.	VIIR	B